Improvement in Emulsifying Capacity of Goose Liver Protein Treated by pH Shifting with Addition of Sodium Tripolyphosphate and Its Proteomics Analysis.

Abstract

Goose liver isolate treated by pH shifting and pH shifting/non-enzyme phosphorylation with goose liver isolate was used as a control. The functional property differences in the protein and proteins involved in the interfacial layer treated with pH shifting and non-enzyme phosphorylation were studied. Compared with the goose protein isolates (GPIs) at pH 7.0, the GPIs treated by pH shifting was not a good choice to be an emulsifier in a neutral environment, and non-enzyme phosphorylation inhibited the negative effects of pH shifting treatment and improved protein properties. The results of proteomics showed that the identified proteins in the interfacial layer belong to hydrophilic proteins. Non-enzyme phosphorylation increased the abundances of most proteins due to ion strength, including some phosphorylated proteins. Correlation analysis indicated that protein solubility was highly positively related with S0, intrinsic fluorescence, total sulfhydryl, free sulfhydryl, A0A0K1R5T3, R0KA48, R0KFP7, U3J1L1, P01989, R0JSM9, and R0LAD1, and was also highly negatively related with particle size and R0M210, R0M714, and R0LFA3. The emulsifying activity index (EAI) demonstrated highly positive correlation with protein solubility, and was correlated with R0JKI4, R0KK84, R0L1Y3, R0LCM7, A0A068C605, and U3IW62.